ReviewBiochemistry2015
Enzymatic oxidation of methane.
Review in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
88 citing papers in PubMed, 340 citations in OpenAlex.
- Remote allosteric control of single-atom Cu sites in Zr-MOFs enables selective CHScience advances · 2026Article
- RegB/A-dependent redox regulation links iron uptake to methanol metabolism inApplied and environmental microbiology · 2026Article
- Biological conversion of methane to organic molecules: towards a low-carbon bioeconomy.National science review · 2026Review
- Structural and functional annotation of Glaciozyma antarctica hypothetical proteins using integrated modeling pipelines.Extremophiles : life under extreme conditions · 2025Article
- Structures of methane and ammonia monooxygenases in native membranes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Concatenating Microbial, Enzymatic, and Organometallic Catalysis for Integrated Conversion of Renewable Carbon Sources.JACS Au · 2024Review
- Genomic Insights into the Landfill Microbial Community: Denitrifying Activity Supporting One-Carbon Utilization.Applied biochemistry and biotechnology · 2024Article
- Expanding the Clip-and-Cleave Concept: Approaching Enantioselective C-H Hydroxylations by Copper Imine Complexes Using OJournal of the American Chemical Society · 2024Article
- A rationally designed miniature of soluble methane monooxygenase enables rapid and high-yield methanol production in Escherichia coli.Nature communications · 2024Article
- Viral potential to modulate microbial methane metabolism varies by habitat.Nature communications · 2024Article
- Direct Methane Oxidation by Copper- and Iron-Dependent Methane Monooxygenases.Chemical reviews · 2024Review
- Methane biohydroxylation into methanol byFrontiers in bioengineering and biotechnology · 2024Article
- Recent Advances in the Catalytic Conversion of Methane to Methanol: From the Challenges of Traditional Catalysts to the Use of Nanomaterials and Metal-Organic Frameworks.Nanomaterials (Basel, Switzerland) · 2023Review
- Recombinant expression and subcellular targeting of the particulate methane monooxygenase (pMMO) protein components in plants.Scientific reports · 2023Article
- Biosensing systems for the detection and quantification of methane gas.Applied microbiology and biotechnology · 2023Review
- Article
- Stacking of a Cofacially Stacked Iron Phthalocyanine Dimer on Graphite Achieved High Catalytic CHJACS Au · 2023Article
- Efficient catalysts of surface hydrophobic Cu-BTC with coordinatively unsaturated Cu(I) sites for the direct oxidation of methane.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Comparative genomic analysis of Methylocystis sp. MJC1 as a platform strain for polyhydroxybutyrate biosynthesis.PloS one · 2023Article
- Cell-Free Protein Synthesis of Particulate Methane Monooxygenase into Nanodiscs.ACS synthetic biology · 2022Article
28 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Methane monooxygenases (MMOs) are enzymes that catalyze the oxidation of methane to methanol in methanotrophic bacteria. As potential targets for new gas-to-liquid methane bioconversion processes, MMOs have attracted intense attention in recent years. There are two distinct types of MMO, a soluble, cytoplasmic MMO (sMMO) and a membrane-bound, particulate MMO (pMMO). Both oxidize methane at metal centers within a complex, multisubunit scaffold, but the structures, active sites, and chemical mechanisms are completely different. This Current Topic review article focuses on the overall architectures, active site structures, substrate reactivities, protein-protein interactions, and chemical mechanisms of both MMOs, with an emphasis on fundamental aspects. In addition, recent advances, including new details of interactions between the sMMO components, characterization of sMMO intermediates, and progress toward understanding the pMMO metal centers are highlighted. The work summarized here provides a guide for those interested in exploiting MMOs for biotechnological applications.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.